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PDBsum entry 1xnh
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* Residue conservation analysis
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Enzyme class:
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E.C.6.3.1.5
- NAD(+) synthase.
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Reaction:
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deamido-NAD+ + NH4+ + ATP = AMP + diphosphate + NAD+ + H+
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deamido-NAD(+)
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+
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NH4(+)
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+
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ATP
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=
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AMP
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+
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diphosphate
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+
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NAD(+)
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proteins
58:985-988
(2005)
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PubMed id:
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Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori.
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G.B.Kang,
Y.S.Kim,
Y.J.Im,
S.H.Rho,
J.H.Lee,
S.H.Eom.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. Structure of H. pylori NAD^+ synthetase. (A) Stereo
view of a ribbon diagram showing the dimeric structure of NAD^+
synthetase. The -helices
are labeled A-
L,
and the -strands
are labeled A-
D.
The two subunits are colored green and blue. The bound NaAD and
ATP molecules are shown as the ball-and-stick models. The red
line indicates a flexible loop region (residued 179-191). (B)
Stereo view of the ATP binding site. Residues of the P-loop are
colored cyan. (C) Stereo view of the NaAD binding site.
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Figure 2.
Figure 2. The multiple sequence alignment of H. pylori, B.
subtilis, and human NAD^+ synthetases. Sequences were aligned
using ClustalX. Highly conserved residues are shaded in black
and gray. The secondary structure elements of NAD^+ synthetase
are indicated by arrows ( -strands),
bars ( -helices),
and lines (connecting loop). Residues constituting ATP and NaAD
binding sites are indicated by open and filled circles,
respectively.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
58,
985-988)
copyright 2005.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Bi,
H.Wang,
and
J.Xie
(2011).
Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets.
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J Cell Physiol,
226,
331-340.
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H.M.McDonald,
P.S.Pruett,
C.Deivanayagam,
I.I.Protasevich,
W.M.Carson,
L.J.DeLucas,
W.J.Brouillette,
and
C.G.Brouillette
(2007).
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis.
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Acta Crystallogr D Biol Crystallogr,
63,
891-905.
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PDB codes:
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J.A.Khan,
X.Tao,
and
L.Tong
(2006).
Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents.
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Nat Struct Mol Biol,
13,
582-588.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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